The objectives of this project are the determination of the structure of bacterial alkaline phosphatase from E. coli by X-ray diffraction methods; the improvement of the structure and X-ray phases of bovine pancreatic ribonuclease-S, the study of small molecule complexes with these enzymes, and development of new techniques in such X-ray analysis. The AP project is at the stage of collecting data from a newly found heavy atom derivative to improve the phases and thus improve the 2.8 A resolution map. Dimercury acetate is the derivative and it was made possible by replacing the (NH4)2SO4 in the crystal with Li2SO4. The ribonuclease refinement is largely a matter of computation but it is also intended to collect new data at lower pH, lower temperature, and on new derivatives. One of the RNase ligands to be studied is a vanadyl-uridine complex which is thought to be an analog of the substrate-product intermediate. The main technical innovation being developed is the use of a convergent beam from an extended X-ray source to produce diffraction similar to a rotation of the crystal. Considerable gain in speed is possible with the use of high powered sources. Alternatively, gain in accessibility to equipment and in economy are possible by using a simple sealed X-ray tube instead of the more costly rotating anode source.